HEADER HYDROLASE 26-JAN-04 1S6O
TITLE SOLUTION STRUCTURE AND BACKBONE DYNAMICS OF THE APO-FORM OF THE SECOND
TITLE 2 METAL-BINDING DOMAIN OF THE MENKES PROTEIN ATP7A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: COPPER-TRANSPORTING ATPASE 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SECOND SOLUBLE DOMAIN;
COMPND 5 SYNONYM: COPPER PUMP 1, MENKES DISEASE-ASSOCIATED PROTEIN;
COMPND 6 EC: 3.6.3.4;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: ATP7A, MNK, MC1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET20B+
KEYWDS COPPER HOMEOSTASIS, METAL TRANSPORT, MENKES, STRUCTURAL PROTEOMICS IN
KEYWDS 2 EUROPE, SPINE, STRUCTURAL GENOMICS, HYDROLASE
EXPDTA SOLUTION NMR
NUMMDL 30
AUTHOR L.BANCI,I.BERTINI,R.DEL CONTE,M.D'ONOFRIO,A.ROSATO,STRUCTURAL
AUTHOR 2 PROTEOMICS IN EUROPE (SPINE)
REVDAT 3 02-MAR-22 1S6O 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1S6O 1 VERSN
REVDAT 1 06-APR-04 1S6O 0
JRNL AUTH L.BANCI,I.BERTINI,R.DEL CONTE,M.D'ONOFRIO,A.ROSATO
JRNL TITL SOLUTION STRUCTURE AND BACKBONE DYNAMICS OF THE CU(I) AND
JRNL TITL 2 APO FORMS OF THE SECOND METAL-BINDING DOMAIN OF THE MENKES
JRNL TITL 3 PROTEIN ATP7A.
JRNL REF BIOCHEMISTRY V. 43 3396 2004
JRNL REFN ISSN 0006-2960
JRNL PMID 15035611
JRNL DOI 10.1021/BI036042S
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DYANA 1.5, DYANA 1.5
REMARK 3 AUTHORS : GUENTERT (DYANA), GUENTERT (DYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1S6O COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-FEB-04.
REMARK 100 THE DEPOSITION ID IS D_1000021434.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : PHOSPHATE 100 MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1 MM PROTEIN, PH 7; 1 MM PROTEIN
REMARK 210 U-15N, PH 7; 1 MM PROTEIN U-15N,
REMARK 210 13C, PH 7
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : [1H-1H]-NOESY; 13C-NOESY-HSQC;
REMARK 210 15N-NOESY-HSQC; HNHA
REMARK 210 SPECTROMETER FIELD STRENGTH : NULL
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : RESTRAINED ENERGY MINIMIZATION
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 30
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: NULL
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 1 THR A 13 24.13 46.92
REMARK 500 1 SER A 16 21.20 -149.67
REMARK 500 1 THR A 18 -78.01 -121.30
REMARK 500 1 HIS A 50 -57.26 -149.36
REMARK 500 1 VAL A 54 -60.21 72.28
REMARK 500 1 LYS A 71 -61.01 -98.57
REMARK 500 2 THR A 13 24.13 46.92
REMARK 500 2 SER A 16 21.20 -149.67
REMARK 500 2 THR A 18 -78.01 -121.30
REMARK 500 2 HIS A 50 -57.26 -149.36
REMARK 500 2 VAL A 54 -60.21 72.28
REMARK 500 2 LYS A 71 -61.01 -98.57
REMARK 500 3 VAL A 9 60.32 -115.05
REMARK 500 3 CYS A 14 -81.48 -77.39
REMARK 500 3 HIS A 15 130.90 -170.62
REMARK 500 3 THR A 18 -69.61 -135.59
REMARK 500 3 LEU A 38 -67.93 -95.87
REMARK 500 3 GLN A 41 18.82 55.06
REMARK 500 3 HIS A 50 -57.00 -139.58
REMARK 500 3 VAL A 54 -65.74 71.13
REMARK 500 3 LYS A 71 -73.21 -78.52
REMARK 500 4 CYS A 14 122.51 68.00
REMARK 500 4 HIS A 15 103.48 -47.85
REMARK 500 4 SER A 16 -64.49 -170.03
REMARK 500 4 THR A 18 -75.71 -136.09
REMARK 500 4 GLN A 29 108.00 -54.69
REMARK 500 4 HIS A 50 -62.28 -146.84
REMARK 500 4 VAL A 54 -59.63 68.64
REMARK 500 4 ALA A 68 -169.24 -108.79
REMARK 500 4 LYS A 71 -94.46 -73.22
REMARK 500 5 GLU A 2 84.10 7.23
REMARK 500 5 THR A 13 -33.03 -132.84
REMARK 500 5 SER A 16 -85.29 -168.39
REMARK 500 5 THR A 18 -80.26 -132.55
REMARK 500 5 GLN A 29 106.06 -56.54
REMARK 500 5 PRO A 49 75.06 -69.43
REMARK 500 5 HIS A 50 -54.55 -140.52
REMARK 500 5 VAL A 54 -56.69 74.02
REMARK 500 5 LYS A 71 -77.77 -88.03
REMARK 500 6 VAL A 9 71.01 -116.30
REMARK 500 6 THR A 13 -170.59 50.78
REMARK 500 6 CYS A 14 156.20 65.40
REMARK 500 6 HIS A 15 39.52 -79.73
REMARK 500 6 SER A 16 108.14 -171.00
REMARK 500 6 CYS A 17 53.44 178.82
REMARK 500 6 THR A 18 -73.52 -130.54
REMARK 500 6 GLN A 29 107.98 -57.97
REMARK 500 6 ASP A 39 -65.05 67.54
REMARK 500 6 HIS A 50 -57.64 -140.01
REMARK 500 6 SER A 53 31.05 -81.57
REMARK 500
REMARK 500 THIS ENTRY HAS 299 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 3 TYR A 47 0.12 SIDE CHAIN
REMARK 500 3 PHE A 69 0.08 SIDE CHAIN
REMARK 500 5 TYR A 47 0.10 SIDE CHAIN
REMARK 500 7 TYR A 47 0.17 SIDE CHAIN
REMARK 500 8 TYR A 47 0.18 SIDE CHAIN
REMARK 500 9 TYR A 47 0.12 SIDE CHAIN
REMARK 500 11 TYR A 47 0.09 SIDE CHAIN
REMARK 500 15 TYR A 47 0.07 SIDE CHAIN
REMARK 500 16 TYR A 47 0.14 SIDE CHAIN
REMARK 500 17 TYR A 47 0.13 SIDE CHAIN
REMARK 500 18 TYR A 47 0.07 SIDE CHAIN
REMARK 500 19 TYR A 47 0.09 SIDE CHAIN
REMARK 500 20 TYR A 47 0.15 SIDE CHAIN
REMARK 500 22 TYR A 47 0.14 SIDE CHAIN
REMARK 500 23 TYR A 47 0.14 SIDE CHAIN
REMARK 500 24 TYR A 47 0.10 SIDE CHAIN
REMARK 500 25 TYR A 47 0.09 SIDE CHAIN
REMARK 500 26 TYR A 47 0.16 SIDE CHAIN
REMARK 500 28 TYR A 47 0.08 SIDE CHAIN
REMARK 500 29 TYR A 47 0.15 SIDE CHAIN
REMARK 500 30 TYR A 47 0.08 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1S6O RELATED DB: PDB
REMARK 900 CU(I) FORM OF THE SECOND METAL-BINDING DOMAIN OF THE MENKES PROTEIN
REMARK 900 ATP7A
REMARK 900 RELATED ID: CIRMMP25 RELATED DB: TARGETDB
DBREF 1S6O A 1 72 UNP Q04656 ATP7A_HUMAN 169 240
SEQADV 1S6O ILE A 73 UNP Q04656 CLONING ARTIFACT
SEQADV 1S6O GLU A 74 UNP Q04656 CLONING ARTIFACT
SEQADV 1S6O GLY A 75 UNP Q04656 CLONING ARTIFACT
SEQADV 1S6O ARG A 76 UNP Q04656 CLONING ARTIFACT
SEQRES 1 A 76 GLY GLU VAL VAL LEU LYS MET LYS VAL GLU GLY MET THR
SEQRES 2 A 76 CYS HIS SER CYS THR SER THR ILE GLU GLY LYS ILE GLY
SEQRES 3 A 76 LYS LEU GLN GLY VAL GLN ARG ILE LYS VAL SER LEU ASP
SEQRES 4 A 76 ASN GLN GLU ALA THR ILE VAL TYR GLN PRO HIS LEU ILE
SEQRES 5 A 76 SER VAL GLU GLU MET LYS LYS GLN ILE GLU ALA MET GLY
SEQRES 6 A 76 PHE PRO ALA PHE VAL LYS LYS ILE GLU GLY ARG
HELIX 1 1 THR A 18 GLY A 26 1 9
HELIX 2 2 GLU A 55 GLY A 65 1 11
SHEET 1 A 4 VAL A 31 SER A 37 0
SHEET 2 A 4 GLU A 42 TYR A 47 -1 O THR A 44 N LYS A 35
SHEET 3 A 4 VAL A 3 LYS A 8 -1 N VAL A 3 O TYR A 47
SHEET 4 A 4 PHE A 69 VAL A 70 -1 O PHE A 69 N LYS A 8
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
MODEL 1
(ATOM LINES ARE NOT SHOWN.)
END
